Purification and some properties of inducible N-acetylglucosamine kinase from Candida albicans

Rai, Y. P. ; Singh, B. ; Elangco, N. ; Datta, A. (1980) Purification and some properties of inducible N-acetylglucosamine kinase from Candida albicans Biochimica et Biophysica Acta (BBA) - Enzymology, 614 (2). pp. 350-356. ISSN 0005-2744

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Official URL: http://linkinghub.elsevier.com/retrieve/pii/000527...

Related URL: http://dx.doi.org/10.1016/0005-2744(80)90224-7


N-Acetylglucosamine kinase (ATP:2-acetamido-2-deoxy-d-glucose 6-phosphotransferase, EC catalyzes the first reaction in the inducible N-acetylglucosamine catabolic pathway of Candida albicans, an obligatory aerobic yeast. As a part of continuing biochemical studies concerning the regulation of gene expression in a simple eukaryote, N-acetylglucosamine kinase has been purified and characterized biochemically. The enzyme has been purified about 300-fold from the crude extract and its molecular weight of 75 000 has been determined by Sephadex G-100 gel filtration. Isolation and analysis procedures are described. The kinase reaction is optimal within a pH range of 7-8. The enzyme is strictly specific for GlcNAc as phosphate acceptor; ATP is the phosphoryl group donor for the kinase reaction and to a lesser extent dATP and CTP. Km values for GlcNAc and ATP are 1.33 mM and 1.82 mM, respectively. The enzyme requires Mg2+, which may be replaced by other bivalent metal ions such as Mn2+, Ca2+, Ba2+ and Co2+ for a lesser degree of effectiveness. The purified enzyme is extremely sensitive to thermal denaturation and becomes completely inactive by heating at 65°C for 2 min. The enzyme is also inactivated by sulphydryl reagents such as p-chloromercuribenzene sulfonic acid and N-ethylmaleimide.

Item Type:Article
Source:Copyright of this article belongs to Elsevier Science.
Keywords:N-acetylglucosamine Kinase; Aminosugar Metabolism; Enzyme Induction; (Yeast)
ID Code:9346
Deposited On:02 Nov 2010 12:24
Last Modified:28 May 2011 10:16

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